2gwc: Difference between revisions

Latest revision as of 08:05, 30 October 2024

Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue

Structural highlights

2gwc is a 8 chain structure with sequence from Brassica juncea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.18Å
Ligands:	BSC, MG, MSE
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSH1_BRAJU Participates in the detoxification process.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Glutathione (GSH) plays a crucial role in plant metabolism and stress response. The rate-limiting step in the biosynthesis of GSH is catalyzed by glutamate cysteine ligase (GCL) the activity of which is tightly regulated. The regulation of plant GCLs is poorly understood. The crystal structure of substrate-bound GCL from Brassica juncea at 2.1-A resolution reveals a plant-unique regulatory mechanism based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of B. juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of B. juncea GCL that is associated with a significant inactivation of the enzyme. These regulatory events provide a molecular link between high GSH levels in the plant cell and associated down-regulation of its biosynthesis. Furthermore, known mutations in the Arabidopsis GCL gene affect residues in the close proximity of the active site and thus explain the decreased GSH levels in mutant plants. In particular, the mutation in rax1-1 plants causes impaired binding of cysteine.

Structural basis for the redox control of plant glutamate cysteine ligase.,Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schafer HJ, Haag-Kerwer A, Rausch T. cDNA cloning and expression analysis of genes encoding GSH synthesis in roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-induction of a putative mitochondrial gamma-glutamylcysteine synthetase isoform. Plant Mol Biol. 1998 May;37(1):87-97. PMID:9620267
↑ Schafer HJ, Greiner S, Rausch T, Haag-Kerwer A. In seedlings of the heavy metal accumulator Brassica juncea Cu2+ differentially affects transcript amounts for gamma-glutamylcysteine synthetase (gamma-ECS) and metallothionein (MT2). FEBS Lett. 1997 Mar 10;404(2-3):216-20. PMID:9119067
↑ Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K. Structural basis for the redox control of plant glutamate cysteine ligase. J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527 doi:10.1074/jbc.M602770200

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Schafer HJ, Haag-Kerwer A, Rausch T. cDNA cloning and expression analysis of genes encoding GSH synthesis in roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-induction of a putative mitochondrial gamma-glutamylcysteine synthetase isoform. Plant Mol Biol. 1998 May;37(1):87-97. PMID:9620267

[2] Schafer HJ, Greiner S, Rausch T, Haag-Kerwer A. In seedlings of the heavy metal accumulator Brassica juncea Cu2+ differentially affects transcript amounts for gamma-glutamylcysteine synthetase (gamma-ECS) and metallothionein (MT2). FEBS Lett. 1997 Mar 10;404(2-3):216-20. PMID:9119067

[3] Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K. Structural basis for the redox control of plant glutamate cysteine ligase. J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527 doi:10.1074/jbc.M602770200

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='2gwc' size='340' side='right'caption='[[2gwc]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gwc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Braju Braju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gwc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_juncea Brassica juncea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BSC:(S)-2-AMINO-4-(AMINO-BUTYLHYDROSULFINYL)BUTANOIC+ACID'>BSC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BSC:(S)-2-AMINO-4-(AMINO-BUTYLHYDROSULFINYL)BUTANOIC+ACID'>BSC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSH1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3707 BRAJU])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--cysteine_ligase Glutamate--cysteine ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.2 6.3.2.2] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwc OCA], [https://pdbe.org/2gwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwc RCSB], [https://www.ebi.ac.uk/pdbsum/2gwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GSH1_BRAJU GSH1_BRAJU]] Participates in the detoxification process.<ref>PMID:9620267</ref> <ref>PMID:9119067</ref>
+[https://www.uniprot.org/uniprot/GSH1_BRAJU GSH1_BRAJU] Participates in the detoxification process.<ref>PMID:9620267</ref> <ref>PMID:9119067</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 15: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gw/2gwc_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 35: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Braju]]
+[[Category: Brassica juncea]]
-[[Category: Glutamate--cysteine ligase]]
 [[Category: Large Structures]]
-[[Category: Gromes, R]]
+[[Category: Gromes R]]
-[[Category: Hothorn, M]]
+[[Category: Hothorn M]]
-[[Category: Rausch, T]]
+[[Category: Rausch T]]
-[[Category: Scheffzek, K]]
+[[Category: Scheffzek K]]
-[[Category: Stuwe, T]]
+[[Category: Stuwe T]]
-[[Category: Wachter, A]]
+[[Category: Wachter A]]
-[[Category: Beta-hairpin]]
-[[Category: Disulfide bridge]]
-[[Category: Glutathione biosynthesis]]
-[[Category: Ligase]]
-[[Category: Redox regulation]]

2gwc: Difference between revisions

Latest revision as of 08:05, 30 October 2024

Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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